N-linked glycosylation of Kv1.2 voltage-gated potassium channel facilitates cell surface expression and enhances the stability of internalized channels

被引：13

作者：

Thayer, Desiree A. ^{[1
,2
,3
,4
]}

Yang, Shi-Bing ^{[1
,2
,3
,5
]}

Jan, Yuh Nung ^{[1
,2
,3
]}

Jan, Lily Y. ^{[1
,2
,3
]}

机构：

[1] Univ Calif San Francisco, Howard Hughes Med Inst, Dept Physiol, San Francisco, CA 94143 USA

[2] Univ Calif San Francisco, Howard Hughes Med Inst, Dept Biochem, San Francisco, CA 94143 USA

[3] Univ Calif San Francisco, Kavli Inst Fundamental Neurosci, Dept Biophys, Weill Inst Neurosci, San Francisco, CA 94143 USA

[4] Amunix, Mountain View, CA USA

[5] Acad Sinica, Inst Biomed Sci, Taipei, Taiwan

来源：

JOURNAL OF PHYSIOLOGY-LONDON | 2016年 / 594卷 / 22期

关键词：

TRAFFICKING;

D O I：

10.1113/JP272394

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

Studies in cultured hippocampal neurons and the COS-7 cell line demonstrate important roles for N-linked glycosylation of Kv1.2 channels in forward trafficking and protein degradation. Kv1.2 channels can contain complex N-linked glycans, which facilitate cell surface expression of the channels. Additionally, the protein stability of cell surface-expressed Kv1.2 channels is affected by glycosylation via differences in the degradation of internalized channels. The present study reveals the importance of N-linked complex glycosylation in boosting Kv1.2 channel density. Notably, sialic acids at the terminal sugar branches play an important role in dampening the degradation of Kv1.2 internalized from the cell membrane to promote its stability.

引用

页码：6701 / 6713

页数：13